Mizuma T, Horie T, Hayashi M, Awazu S
J Pharmacobiodyn. 1986 Mar;9(3):244-8. doi: 10.1248/bpb1978.9.244.
The binding of bovine serum albumin (BSA), containing 125I-BSA, to isolated rat hepatocytes was studied over a 300-fold concentration range of BSA to characterize the interaction between albumin and the liver cells in albumin-mediated hepatic transport. The binding of BSA with a high affinity to the cell surface of hepatocytes was not found in the binding behavior. The bound fraction of BSA with hepatocytes was about 1% over those concentration range of BSA.
研究了含有¹²⁵I-牛血清白蛋白(BSA)的牛血清白蛋白与分离的大鼠肝细胞的结合情况,该研究涵盖了300倍浓度范围的BSA,以表征白蛋白与白蛋白介导的肝脏转运中肝细胞之间的相互作用。在结合行为中未发现BSA与肝细胞表面具有高亲和力的结合。在那些BSA浓度范围内,BSA与肝细胞的结合分数约为1%。